ArticlePloS one2016
Extended Synaptotagmin (ESyt) Triple Knock-Out Mice Are Viable and Fertile without Obvious Endoplasmic Reticulum Dysfunction.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed, 1 synthesis or guideline pooled it, 69 citations in OpenAlex.
- Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024Pooled it
- Lipid metabolism and contact site homologs are present at the chloroplast envelope-thylakoid interface.Nature communications · 2026Article
- MCTP1 and MCTP2 promote ER-PM contact sites and regulate PI4P homeostasis and cell migration.Molecular biology of the cell · 2026Article
- The complex web of membrane contact sites in brain aging and neurodegeneration.Cellular and molecular life sciences : CMLS · 2025Review
- Lipid transporters E-Syt3 and ORP5 regulate epithelial ion transport by controlling phosphatidylserine enrichment at ER/PM junctions.The EMBO journal · 2025Article
- Sphingosine-1-phosphate signalling activates E-Syt1 to facilitate HDL-derived cholesterol transport.Nature cell biology · 2025Article
- ER-plasma membrane contact sites deliver ER lipids and proteins for rapid cell surface expansion.The Journal of cell biology · 2024Article
- Enriched Environment Enhances Sociability Through the Promotion of ESyt1-Related Synaptic Formation in the Medial Prefrontal Cortex.Molecular neurobiology · 2024Article
- Extended-Synaptotagmin-1 and -2 control T cell signaling and function.EMBO reports · 2024Article
- Article
- ESYT1 tethers the ER to mitochondria and is required for mitochondrial lipid and calcium homeostasis.Life science alliance · 2024Article
- The Tricalbin-Family Endoplasmic Reticulum-Plasma Membrane Tethering Proteins Attenuate ROS-Involved Caspofungin Sensitivity in Candida albicans.Microbiology spectrum · 2022Article
- The Role of Lipids in CRAC Channel Function.Biomolecules · 2022Review
- Article
- INPP5K and Atlastin-1 maintain the nonuniform distribution of ER-plasma membrane contacts in neurons.Life science alliance · 2021Article
- Structural studies of the shortest extended synaptotagmin with only two C2 domains fromiScience · 2021Article
- Room for Two: The Synaptophysin/Synaptobrevin Complex.Frontiers in synaptic neuroscience · 2021Article
- Endoplasmic Reticulum-Plasma Membrane Contact Sites: Regulators, Mechanisms, and Physiological Functions.Frontiers in cell and developmental biology · 2021Review
- ER-PM Contact Sites - SNARING Actors in Emerging Functions.Frontiers in cell and developmental biology · 2021Review
- Extended synaptotagmin regulates membrane contact site structure and lipid transfer function in vivo.EMBO reports · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extended synaptotagmins (ESyts) are endoplasmic reticulum (ER) proteins composed of an N-terminal transmembrane region, a central SMP-domain, and five (ESyt1) or three C-terminal cytoplasmic C2-domains (ESyt2 and ESyt3). ESyts bind phospholipids in a Ca2+-dependent manner via their C2-domains, are localized to ER-plasma membrane contact sites, and may catalyze lipid exchange between the plasma membrane and the ER via their SMP-domains. However, the overall function of ESyts has remained enigmatic. Here, we generated triple constitutive and conditional knock-out mice that lack all three ESyt isoforms; in addition, we produced knock-in mice that express mutant ESyt1 or ESyt2 carrying inactivating substitutions in the Ca2+-binding sites of their C2A-domains. Strikingly, all ESyt mutant mice, even those lacking all ESyts, were apparently normal and survived and bred in a manner indistinguishable from control mice. ESyt mutant mice displayed no major changes in brain morphology or synaptic protein composition, and exhibited no large alterations in stress responses. Thus, in mice ESyts do not perform an essential role in basic cellular functions, suggesting that these highly conserved proteins may perform a specialized role that may manifest only during specific, as yet untested challenges.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.